ID G2I5T4_KOMMN Unreviewed; 396 AA.
AC G2I5T4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN ECO:0000313|EMBL:BAK83481.1};
GN OrderedLocusNames=GLX_10690 {ECO:0000313|EMBL:BAK83481.1};
OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS Kondo 51) (Gluconacetobacter medellinensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK83481.1, ECO:0000313|Proteomes:UP000009044};
RN [1] {ECO:0000313|Proteomes:UP000009044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC {ECO:0000313|Proteomes:UP000009044};
RX PubMed=22123756; DOI=10.1128/JB.06158-11;
RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT strain of Gluconacetobacter xylinus isolated from vinegar.";
RL J. Bacteriol. 193:6997-6998(2011).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC Rule:MF_00118}.
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DR EMBL; AP012159; BAK83481.1; -; Genomic_DNA.
DR RefSeq; WP_014105031.1; NC_016027.1.
DR AlphaFoldDB; G2I5T4; -.
DR STRING; 634177.GLX_10690; -.
DR KEGG; gxy:GLX_10690; -.
DR PATRIC; fig|634177.7.peg.1228; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_5; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000009044; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}.
FT DOMAIN 10..206
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 396 AA; 43065 MW; F7A63F999F732B91 CRC64;
MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKTLAKSG GAEFKAYDMI DAAPEERARG
ITISTAHVEY ETAKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLARQVGVPA LVVFLNKVDQ VDDPELLELV EMEVRELLSA YQFPGDDIPI IKGSALVTLE
DGDPEVGENR VLDLMNAVDE YIPQPERPVD RPFLMPIEDV FSISGRGTVV TGRVERGVVN
VGDEIEIVGL RPTQKTTVTG VEMFRKLLDR GEAGDNIGAL VRGTKREDVE RGQVLAKPGS
ITPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNVA
MDVELIAPIA MDEGLRFAIR EGGRTVGAGV VASITA
//